BMRB Entry 30088

Name: Solid-state MAS NMR structure of beta 1 domain of protein G (GB1)
Published: 2016-08-08

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PDB ID: 5jxv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30088
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solid-state MAS NMR structure of beta 1 domain of protein G (GB1) PubMed: 27489348

Deposition date: 2016-05-13 Original release date: 2016-08-08

Authors: Andreas, L.; Jaudzems, K.; Stanek, J.; Lalli, D.; Bertarello, A.; Le Marchand, T.; Cala-De Paepe, D.; Kotelovica, S.; Akopjana, I.; Knott, B.; Wegner, S.; Engelke, F.; Lesage, A.; Emsley, L.; Tars, K.; Herrmann, T.; Pintacuda, G.

Citation: Andreas, Loren; Jaudzems, Kristaps; Stanek, Jan; Lalli, Daniela; Bertarello, Andrea; Marchand, Tanguy; Paepe, Diane; Kotelovica, Svetlana; Akopjana, Inara; Knott, Benno; Wegner, Sebastian; Engelke, Frank; Lesage, Anne; Emsley, Lyndon; Tars, Kaspars; Herrmann, Torsten; Pintacuda, Guido. "Structure of fully protonated proteins by proton-detected magic-angle spinning NMR" Proc. Natl. Acad. Sci. U. S. A. 113, 9187-9192 (2016).

Assembly members:
Immunoglobulin G-binding protein G, polymer, 56 residues, 6228.809 Da.

Natural source: Common Name: firmicutes Taxonomy ID: 119602 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus Streptococcus dysgalactiae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Immunoglobulin G-binding protein G: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	224
15N chemical shifts	65
1H chemical shifts	360

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 56 residues - 6228.809 Da.

1

MET

GLN

TYR

LYS

LEU

ILE

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

4

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: B1 domain of Immunoglobulin G-Binding protein G, [U-99% 13C; U-99% 15N], 800 ± 300 mg/mL; isopropyl alcohol 22.5 ± 5 %; methyl-2,4-pentane diol 45 ± 5 %; sodium phosphate 12.5 ± 5 mM

sample_conditions_1: ionic strength: 12.5 mM; pH: 5.6; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
(H)NCAH	sample_1	isotropic	sample_conditions_1
(H)CANH	sample_1	isotropic	sample_conditions_1
(H)(CO)CA(CO)NH	sample_1	isotropic	sample_conditions_1
(H)(CA)CB(CA)NH	sample_1	isotropic	sample_conditions_1
(H)N(CA)(CO)NH	sample_1	isotropic	sample_conditions_1
(H)N(CO)(CA)NH	sample_1	isotropic	sample_conditions_1
(H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
(H)NHH-RFDR	sample_1	isotropic	sample_conditions_1
(H)CHH-RFDR	sample_1	isotropic	sample_conditions_1
H(H)CH-RFDR-aromatic13C	sample_1	isotropic	sample_conditions_1

Software:

CANDID v2.6.0, Herrmann, Guntert and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 1000 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts